Internalization of the type I angiotensin II receptor (AT1) is required for protein kinase C activation but not for inositol trisphosphate release in the angiotensin II stimulated rat adrenal zona glomerulosa cell

Biochem Biophys Res Commun. 1994 Nov 15;204(3):1292-8. doi: 10.1006/bbrc.1994.2603.

Abstract

A specific antibody, 6313/G2, to the N-terminus of the angiotensin II type I (AT1) receptor causes retention of the AT1 receptor in the plasma membrane of rat adrenal zona glomerulosa cells and stimulates steroidogenesis and inositol trisphosphate (IP3) release. Its effects are not significantly additive with those of angiotensin. In contrast, 6313/G2 completely inhibits angiotensin induced translocation of protein kinase C to the membrane fraction, although alone it has no effect. The data suggest that IP3 linked events, such as steroidogenesis, do not require receptor internalization, but protein kinase C activation does. They also confirm that protein kinase C activation is not required for stimulation of steroidogenesis in rat dispersed glomerulosa cells.

MeSH terms

  • Aldosterone / biosynthesis*
  • Angiotensin II / pharmacology*
  • Animals
  • Antibodies, Monoclonal / pharmacology
  • Cell Membrane / metabolism
  • Cyclic AMP / metabolism
  • Enzyme Activation
  • Female
  • In Vitro Techniques
  • Inositol 1,4,5-Trisphosphate / metabolism*
  • Kinetics
  • Male
  • Protein Kinase C / metabolism*
  • Rats
  • Rats, Wistar
  • Receptors, Angiotensin / metabolism*
  • Zona Glomerulosa / drug effects
  • Zona Glomerulosa / metabolism*

Substances

  • Antibodies, Monoclonal
  • Receptors, Angiotensin
  • Angiotensin II
  • Aldosterone
  • Inositol 1,4,5-Trisphosphate
  • Cyclic AMP
  • Protein Kinase C